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P20594

- ANPRB_HUMAN

UniProt

P20594 - ANPRB_HUMAN

Protein

Atrial natriuretic peptide receptor 2

Gene

NPR2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 168 (01 Oct 2014)
      Sequence version 1 (01 Feb 1991)
      Previous versions | rss
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    Functioni

    Receptor for the C-type natriuretic peptide NPPC/CNP hormone. Has guanylate cyclase activity upon binding of its ligand. May play a role in the regulation of skeletal growth.2 Publications

    Catalytic activityi

    GTP = 3',5'-cyclic GMP + diphosphate.

    GO - Molecular functioni

    1. ATP binding Source: Ensembl
    2. GTP binding Source: UniProtKB-KW
    3. guanylate cyclase activity Source: UniProtKB
    4. hormone binding Source: UniProtKB
    5. natriuretic peptide receptor activity Source: UniProtKB
    6. peptide hormone binding Source: Ensembl
    7. protein kinase activity Source: InterPro
    8. receptor activity Source: ProtInc
    9. transmembrane signaling receptor activity Source: ProtInc

    GO - Biological processi

    1. bone development Source: Ensembl
    2. cell surface receptor signaling pathway Source: ProtInc
    3. cellular response to granulocyte macrophage colony-stimulating factor stimulus Source: UniProtKB
    4. cGMP biosynthetic process Source: UniProtKB
    5. intracellular signal transduction Source: InterPro
    6. ossification Source: UniProtKB-KW
    7. receptor guanylyl cyclase signaling pathway Source: UniProtKB
    8. regulation of blood pressure Source: ProtInc
    9. signal transduction Source: ProtInc

    Keywords - Molecular functioni

    Lyase, Receptor

    Keywords - Biological processi

    cGMP biosynthesis, Osteogenesis

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Atrial natriuretic peptide receptor 2 (EC:4.6.1.2)
    Alternative name(s):
    Atrial natriuretic peptide receptor type B
    Short name:
    ANP-B
    Short name:
    ANPR-B
    Short name:
    NPR-B
    Guanylate cyclase B
    Short name:
    GC-B
    Gene namesi
    Name:NPR2
    Synonyms:ANPRB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:7944. NPR2.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: ProtInc

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Acromesomelic dysplasia, Maroteaux type (AMDM) [MIM:602875]: An autosomal recessive acromesomelic chondrodysplasia. Acromesomelic chondrodysplasias are rare hereditary skeletal disorders characterized by short stature, very short limbs and hand/foot malformations. The severity of limb abnormalities increases from proximal to distal with profoundly affected hands and feet showing brachydactyly and/or rudimentary fingers (knob-like fingers). AMDM is characterized by axial skeletal involvement with wedging of vertebral bodies. In AMDM all skeletal elements are present but show abnormal rates of linear growth.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti32 – 321P → T in AMDM. 1 Publication
    Corresponds to variant rs28931581 [ dbSNP | Ensembl ].
    VAR_022583
    Natural varianti115 – 1151W → G in AMDM; markedly deficient activity. 1 Publication
    Corresponds to variant rs28931582 [ dbSNP | Ensembl ].
    VAR_022584
    Natural varianti176 – 1761D → E in AMDM. 1 Publication
    Corresponds to variant rs28929479 [ dbSNP | Ensembl ].
    VAR_022585
    Natural varianti297 – 2971T → M in AMDM; markedly deficient activity. 1 Publication
    VAR_022586
    Natural varianti338 – 3381Y → C in AMDM. 1 Publication
    VAR_022587
    Natural varianti409 – 4091A → T in AMDM. 1 Publication
    VAR_022588
    Natural varianti413 – 4131G → E in AMDM; markedly deficient activity. 1 Publication
    VAR_022589
    Natural varianti708 – 7081Y → C in AMDM. 1 Publication
    VAR_022590
    Natural varianti776 – 7761R → W in AMDM. 1 Publication
    VAR_022591
    Natural varianti957 – 9571R → C in AMDM. 1 Publication
    VAR_022592
    Natural varianti959 – 9591G → A in AMDM. 1 Publication
    VAR_022593

    Keywords - Diseasei

    Disease mutation, Dwarfism

    Organism-specific databases

    MIMi602875. phenotype.
    Orphaneti40. Acromesomelic dysplasia, Maroteaux type.
    329191. Tall stature - scoliosis - macrodactyly of the great toes.
    PharmGKBiPA257.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 10471025Atrial natriuretic peptide receptor 2PRO_0000012364Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi24 – 241N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi35 – 351N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi75 ↔ 101By similarity
    Glycosylationi161 – 1611N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi195 – 1951N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi244 – 2441N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi277 – 2771N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi349 – 3491N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi439 – 439InterchainCurated
    Disulfide bondi448 – 448InterchainCurated
    Modified residuei513 – 5131Phosphoserine1 Publication
    Modified residuei516 – 5161Phosphothreonine1 Publication
    Modified residuei518 – 5181Phosphoserine1 Publication
    Modified residuei523 – 5231Phosphoserine1 Publication
    Modified residuei526 – 5261Phosphoserine1 Publication
    Modified residuei529 – 5291Phosphothreonine1 Publication

    Post-translational modificationi

    Phosphorylation of the protein kinase-like domain is required for full activation by CNP.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP20594.
    PaxDbiP20594.
    PRIDEiP20594.

    PTM databases

    PhosphoSiteiP20594.

    Expressioni

    Gene expression databases

    ArrayExpressiP20594.
    BgeeiP20594.
    CleanExiHS_NPR2.
    GenevestigatoriP20594.

    Organism-specific databases

    HPAiHPA011977.

    Interactioni

    Protein-protein interaction databases

    BioGridi110942. 4 interactions.
    IntActiP20594. 2 interactions.
    STRINGi9606.ENSP00000341083.

    Structurei

    3D structure databases

    ProteinModelPortaliP20594.
    SMRiP20594. Positions 24-442, 503-832, 854-1036.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini23 – 458436ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini479 – 1047569CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei459 – 47820HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini513 – 786274Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini861 – 991131Guanylate cyclasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the adenylyl cyclase class-4/guanylyl cyclase family.PROSITE-ProRule annotation
    Contains 1 guanylate cyclase domain.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG051862.
    InParanoidiP20594.
    KOiK12324.
    OMAiAAKSEHY.
    OrthoDBiEOG7Z69BJ.
    PhylomeDBiP20594.
    TreeFamiTF106338.

    Family and domain databases

    Gene3Di3.30.70.1230. 1 hit.
    InterProiIPR001054. A/G_cyclase.
    IPR018297. A/G_cyclase_CS.
    IPR001828. ANF_lig-bd_rcpt.
    IPR011009. Kinase-like_dom.
    IPR001170. Ntpep_rcpt.
    IPR028082. Peripla_BP_I.
    IPR000719. Prot_kinase_dom.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    [Graphical view]
    PfamiPF01094. ANF_receptor. 1 hit.
    PF00211. Guanylate_cyc. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view]
    PRINTSiPR00255. NATPEPTIDER.
    SMARTiSM00044. CYCc. 1 hit.
    [Graphical view]
    SUPFAMiSSF53822. SSF53822. 1 hit.
    SSF55073. SSF55073. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS00458. ANF_RECEPTORS. 1 hit.
    PS00452. GUANYLATE_CYCLASE_1. 1 hit.
    PS50125. GUANYLATE_CYCLASE_2. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: P20594-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MALPSLLLLV AALAGGVRPP GARNLTLAVV LPEHNLSYAW AWPRVGPAVA     50
    LAVEALGRAL PVDLRFVSSE LEGACSEYLA PLSAVDLKLY HDPDLLLGPG 100
    CVYPAASVAR FASHWRLPLL TAGAVASGFS AKNDHYRTLV RTGPSAPKLG 150
    EFVVTLHGHF NWTARAALLY LDARTDDRPH YFTIEGVFEA LQGSNLSVQH 200
    QVYAREPGGP EQATHFIRAN GRIVYICGPL EMLHEILLQA QRENLTNGDY 250
    VFFYLDVFGE SLRAGPTRAT GRPWQDNRTR EQAQALREAF QTVLVITYRE 300
    PPNPEYQEFQ NRLLIRARED FGVELGPSLM NLIAGCFYDG ILLYAEVLNE 350
    TIQEGGTRED GLRIVEKMQG RRYHGVTGLV VMDKNNDRET DFVLWAMGDL 400
    DSGDFQPAAH YSGAEKQIWW TGRPIPWVKG APPSDNPPCA FDLDDPSCDK 450
    TPLSTLAIVA LGTGITFIMF GVSSFLIFRK LMLEKELASM LWRIRWEELQ 500
    FGNSERYHKG AGSRLTLSLR GSSYGSLMTA HGKYQIFANT GHFKGNVVAI 550
    KHVNKKRIEL TRQVLFELKH MRDVQFNHLT RFIGACIDPP NICIVTEYCP 600
    RGSLQDILEN DSINLDWMFR YSLINDLVKG MAFLHNSIIS SHGSLKSSNC 650
    VVDSRFVLKI TDYGLASFRS TAEPDDSHAL YAKKLWTAPE LLSGNPLPTT 700
    GMQKADVYSF GIILQEIALR SGPFYLEGLD LSPKEIVQKV RNGQRPYFRP 750
    SIDRTQLNEE LVLLMERCWA QDPAERPDFG QIKGFIRRFN KEGGTSILDN 800
    LLLRMEQYAN NLEKLVEERT QAYLEEKRKA EALLYQILPH SVAEQLKRGE 850
    TVQAEAFDSV TIYFSDIVGF TALSAESTPM QVVTLLNDLY TCFDAIIDNF 900
    DVYKVETIGD AYMVVSGLPG RNGQRHAPEI ARMALALLDA VSSFRIRHRP 950
    HDQLRLRIGV HTGPVCAGVV GLKMPRYCLF GDTVNTASRM ESNGQALKIH 1000
    VSSTTKDALD ELGCFQLELR GDVEMKGKGK MRTYWLLGER KGPPGLL 1047
    Length:1,047
    Mass (Da):117,022
    Last modified:February 1, 1991 - v1
    Checksum:i817FB74D6B31F7EF
    GO
    Isoform Short (identifier: P20594-2) [UniParc]FASTAAdd to Basket

    Also known as: NPR-BI

    The sequence of this isoform differs from the canonical sequence as follows:
         964-1047: PVCAGVVGLK...GERKGPPGLL → KADSHSSPSLHLSQTLPTCFFSKGQSVLGLLA

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:995
    Mass (Da):111,208
    Checksum:i745D41E451E0D7DF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti755 – 7551T → S in BAA81737. (PubMed:10082481)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti32 – 321P → T in AMDM. 1 Publication
    Corresponds to variant rs28931581 [ dbSNP | Ensembl ].
    VAR_022583
    Natural varianti115 – 1151W → G in AMDM; markedly deficient activity. 1 Publication
    Corresponds to variant rs28931582 [ dbSNP | Ensembl ].
    VAR_022584
    Natural varianti176 – 1761D → E in AMDM. 1 Publication
    Corresponds to variant rs28929479 [ dbSNP | Ensembl ].
    VAR_022585
    Natural varianti232 – 2321M → I.1 Publication
    Corresponds to variant rs55747238 [ dbSNP | Ensembl ].
    VAR_042219
    Natural varianti297 – 2971T → M in AMDM; markedly deficient activity. 1 Publication
    VAR_022586
    Natural varianti338 – 3381Y → C in AMDM. 1 Publication
    VAR_022587
    Natural varianti409 – 4091A → T in AMDM. 1 Publication
    VAR_022588
    Natural varianti413 – 4131G → E in AMDM; markedly deficient activity. 1 Publication
    VAR_022589
    Natural varianti708 – 7081Y → C in AMDM. 1 Publication
    VAR_022590
    Natural varianti771 – 7711Q → E.
    Corresponds to variant rs5816 [ dbSNP | Ensembl ].
    VAR_011968
    Natural varianti776 – 7761R → W in AMDM. 1 Publication
    VAR_022591
    Natural varianti882 – 8821V → I.1 Publication
    Corresponds to variant rs55700371 [ dbSNP | Ensembl ].
    VAR_042220
    Natural varianti957 – 9571R → C in AMDM. 1 Publication
    VAR_022592
    Natural varianti959 – 9591G → A in AMDM. 1 Publication
    VAR_022593

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei964 – 104784PVCAG…PPGLL → KADSHSSPSLHLSQTLPTCF FSKGQSVLGLLA in isoform Short. 1 PublicationVSP_001810Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB005647 Genomic DNA. Translation: BAA81737.1.
    AJ005282 mRNA. Translation: CAA06466.1.
    AL133410 Genomic DNA. Translation: CAI10987.1.
    EU326311 Genomic DNA. Translation: ACA05920.1.
    EU326311 Genomic DNA. Translation: ACA05921.1.
    CH471071 Genomic DNA. Translation: EAW58338.1.
    CH471071 Genomic DNA. Translation: EAW58337.1.
    CH471071 Genomic DNA. Translation: EAW58339.1.
    CH471071 Genomic DNA. Translation: EAW58340.1.
    BC023017 mRNA. Translation: AAH23017.1.
    CCDSiCCDS6590.1. [P20594-1]
    PIRiS05514. OYHUBR.
    RefSeqiNP_003986.2. NM_003995.3. [P20594-1]
    UniGeneiHs.78518.

    Genome annotation databases

    EnsembliENST00000342694; ENSP00000341083; ENSG00000159899. [P20594-1]
    GeneIDi4882.
    KEGGihsa:4882.
    UCSCiuc003zyd.3. human. [P20594-1]

    Polymorphism databases

    DMDMi113916.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB005647 Genomic DNA. Translation: BAA81737.1 .
    AJ005282 mRNA. Translation: CAA06466.1 .
    AL133410 Genomic DNA. Translation: CAI10987.1 .
    EU326311 Genomic DNA. Translation: ACA05920.1 .
    EU326311 Genomic DNA. Translation: ACA05921.1 .
    CH471071 Genomic DNA. Translation: EAW58338.1 .
    CH471071 Genomic DNA. Translation: EAW58337.1 .
    CH471071 Genomic DNA. Translation: EAW58339.1 .
    CH471071 Genomic DNA. Translation: EAW58340.1 .
    BC023017 mRNA. Translation: AAH23017.1 .
    CCDSi CCDS6590.1. [P20594-1 ]
    PIRi S05514. OYHUBR.
    RefSeqi NP_003986.2. NM_003995.3. [P20594-1 ]
    UniGenei Hs.78518.

    3D structure databases

    ProteinModelPortali P20594.
    SMRi P20594. Positions 24-442, 503-832, 854-1036.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110942. 4 interactions.
    IntActi P20594. 2 interactions.
    STRINGi 9606.ENSP00000341083.

    Chemistry

    BindingDBi P20594.
    ChEMBLi CHEMBL2111337.
    DrugBanki DB01613. Erythrityl Tetranitrate.
    DB04899. Nesiritide.
    GuidetoPHARMACOLOGYi 1748.

    PTM databases

    PhosphoSitei P20594.

    Polymorphism databases

    DMDMi 113916.

    Proteomic databases

    MaxQBi P20594.
    PaxDbi P20594.
    PRIDEi P20594.

    Protocols and materials databases

    DNASUi 4882.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000342694 ; ENSP00000341083 ; ENSG00000159899 . [P20594-1 ]
    GeneIDi 4882.
    KEGGi hsa:4882.
    UCSCi uc003zyd.3. human. [P20594-1 ]

    Organism-specific databases

    CTDi 4882.
    GeneCardsi GC09P035792.
    H-InvDB HIX0034787.
    HGNCi HGNC:7944. NPR2.
    HPAi HPA011977.
    MIMi 108961. gene.
    602875. phenotype.
    neXtProti NX_P20594.
    Orphaneti 40. Acromesomelic dysplasia, Maroteaux type.
    329191. Tall stature - scoliosis - macrodactyly of the great toes.
    PharmGKBi PA257.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOVERGENi HBG051862.
    InParanoidi P20594.
    KOi K12324.
    OMAi AAKSEHY.
    OrthoDBi EOG7Z69BJ.
    PhylomeDBi P20594.
    TreeFami TF106338.

    Miscellaneous databases

    ChiTaRSi NPR2. human.
    GeneWikii NPR2.
    GenomeRNAii 4882.
    NextBioi 18792.
    PROi P20594.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P20594.
    Bgeei P20594.
    CleanExi HS_NPR2.
    Genevestigatori P20594.

    Family and domain databases

    Gene3Di 3.30.70.1230. 1 hit.
    InterProi IPR001054. A/G_cyclase.
    IPR018297. A/G_cyclase_CS.
    IPR001828. ANF_lig-bd_rcpt.
    IPR011009. Kinase-like_dom.
    IPR001170. Ntpep_rcpt.
    IPR028082. Peripla_BP_I.
    IPR000719. Prot_kinase_dom.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    [Graphical view ]
    Pfami PF01094. ANF_receptor. 1 hit.
    PF00211. Guanylate_cyc. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view ]
    PRINTSi PR00255. NATPEPTIDER.
    SMARTi SM00044. CYCc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53822. SSF53822. 1 hit.
    SSF55073. SSF55073. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS00458. ANF_RECEPTORS. 1 hit.
    PS00452. GUANYLATE_CYCLASE_1. 1 hit.
    PS50125. GUANYLATE_CYCLASE_2. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Differential activation by atrial and brain natriuretic peptides of two different receptor guanylate cyclases."
      Chang M.S., Lowe D.G., Lewis M., Hellmiss R., Chen E., Goeddel D.V.
      Nature 341:68-72(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE (ISOFORM LONG).
      Tissue: Brain.
    2. "Structure of the type B human natriuretic peptide receptor gene and association of a novel microsatellite polymorphism with essential hypertension."
      Rehemudula D., Nakayama T., Soma M., Takahashi Y., Uwabo J., Sato M., Izumi Y., Kanmatsuse K., Ozawa Y.
      Circ. Res. 84:605-610(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Blood.
    3. "cGMP-dependent and -independent inhibition of a K+ conductance by natriuretic peptides: molecular and functional studies in human proximal tubule cells."
      Hirsch J.R., Meyer M., Maegert H.-J., Forssmann W.-G., Mollerup S., Herter P., Weber G., Cermak R., Ankorina-Stark I., Schlatter E., Kruhoffer M.
      J. Am. Soc. Nephrol. 10:472-480(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
      Tissue: Kidney.
    4. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. NHLBI resequencing and genotyping service (RS&G)
      Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
      Tissue: Brain.
    8. "Extracellular domain-IgG fusion proteins for three human natriuretic peptide receptors. Hormone pharmacology and application to solid phase screening of synthetic peptide antisera."
      Bennett B.D., Bennett G.L., Vitangcol R.V., Jewett J.R., Burnier J., Henzel W., Lowe D.G.
      J. Biol. Chem. 266:23060-23067(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: LIGAND-BINDING.
    9. "Selective activation of the B natriuretic peptide receptor by C-type natriuretic peptide (CNP)."
      Koller K.J., Lowe D.G., Bennett G.L., Minamino N., Kangawa K., Matsuo H., Goeddel D.V.
      Science 252:120-123(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
    11. Cited for: FUNCTION, VARIANTS AMDM THR-32; GLY-115; GLU-176; MET-297; CYS-338; THR-409; GLU-413; CYS-708; TRP-776; CYS-957 AND ALA-959, CHARACTERIZATION OF VARIANTS AMDM GLY-115; MET-297 AND GLU-413.
    12. "Mass spectrometric identification of phosphorylation sites in guanylyl cyclase A and B."
      Yoder A.R., Stone M.D., Griffin T.J., Potter L.R.
      Biochemistry 49:10137-10145(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-513; THR-516; SER-518; SER-523; SER-526 AND THR-529.
    13. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] ILE-232 AND ILE-882.

    Entry informationi

    Entry nameiANPRB_HUMAN
    AccessioniPrimary (citable) accession number: P20594
    Secondary accession number(s): B0ZBF2
    , B0ZBF3, D3DRP3, D3DRP4, O60871, Q4VAK7, Q5TCV2, Q8TA93, Q9UQ50
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 168 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3